asparagine and guanosine triphosphate

asparagine has been researched along with guanosine triphosphate in 28 studies

Research

Studies (28)

TimeframeStudies, this research(%)All Research%
pre-19905 (17.86)18.7374
1990's11 (39.29)18.2507
2000's10 (35.71)29.6817
2010's2 (7.14)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Makarewicz, W1
Kaji, A; Ogawa, K1
Day, R; Farnsworth, CL; Feig, LA; Hildebrandt, JD1
Fujiwara, M; Narumiya, S; Sekine, A1
Cooper, GM; Feig, LA1
Hwang, YW; Miller, DL1
Fromm, HJ; Honzatko, RB; Kang, C; Sun, N1
Farrar, CT; Halkides, CJ; Larsen, RG; Redfield, AG; Singel, DJ1
Gallaher, TK; Shih, JC; Wang, CD1
Bârzu, O; Parmeggiani, A; Sarfati, R; Weijland, A1
Cao, C; Huang, J; Lutkenhaus, J; Mukherjee, A; Wang, X1
Clark, BF; Knudsen, CR; Nautrup Pedersen, G; Rattenborg, T1
Finken-Eigen, M; Köhrer, K; Müller, S1
Blumer, KJ; Overton, MC; Srinivasa, SP; Watson, N1
Lannigan, DA; Macara, IG; Tatsis, N1
Gilman, AG; Mukhopadhyay, S; Posner, BA; Ross, EM; Tesmer, JJ1
Bienengraeber, M; Echtay, KS; Klingenberg, M; Winkler, E1
Brannetti, B; Ferrè, F; Helmer-Citterich, M; Valencia, A; Via, A1
Brito, M; Guzmán, L; Hinrichs, MV; Olate, J; Romo, X; Soto, X1
Cerione, RA; Hahn, K; Nolbant, P; Tu, SS; Wu, WJ; Yang, W1
Bos, JL; Rehmann, H1
Chakrabarti, PP; Daumke, O; Vetter, IR; Weyand, M; Wittinghofer, A1
Arnold, E; Ding, J; Guan, K; Li, S; Li, Y; Xu, X; Yu, Y1
Assairi, L; Barzu, O; Briozzo, P; Evrin, C; Gilles, AM; Joly, N; Meyer, P1
Castro, LI; Hermsen, C; Linder, JU; Schultz, JE1
Alifano, P; Bucci, C; De Luca, A; Progida, C; Spinosa, MR1
Garcia-Diaz, M; Nassar, N; Singh, K1
Aasly, JO; Cobb, SA; Dachsel, JC; Farrer, MJ; Felic, A; Haugarvoll, K; Johansen, KK; Kachergus, JM; Lincoln, SJ; Nutt, JG; Payami, H; Ross, OA; Soto-Ortolaza, AI; Toft, M; Vilariño-Güell, C; Webber, PJ; West, AB; White, LR; Wider, C1

Other Studies

28 other study(ies) available for asparagine and guanosine triphosphate

ArticleYear
[The purine nucleotide cycle (author's transl)].
    Postepy biochemii, 1979, Volume: 25, Issue:2

    Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Adenylosuccinate Lyase; Adenylosuccinate Synthase; Amino Acids; AMP Deaminase; Animals; Asparagine; Guanosine Monophosphate; Guanosine Triphosphate; Humans; In Vitro Techniques; Inosine Monophosphate; Muscles; Purine Nucleotides; Rabbits; Rats

1979
Requirement for ribosome-releasing factor for the release of ribosomes at the termination codon.
    European journal of biochemistry, 1975, Oct-15, Volume: 58, Issue:2

    Topics: Amino Acids; Asparagine; Codon; Guanosine Triphosphate; Peptide Elongation Factors; Peptide Initiation Factors; Peptide Termination Factors; Polyribosomes; Puromycin; Ribosomes; RNA, Messenger; RNA, Transfer

1975
A mutation in the putative Mg(2+)-binding site of Gs alpha prevents its activation by receptors.
    Molecular and cellular biology, 1991, Volume: 11, Issue:10

    Topics: Adenylyl Cyclases; Animals; Asparagine; Binding Sites; Blotting, Northern; Cyclic AMP; Enzyme Activation; Gene Expression Regulation, Enzymologic; GTP-Binding Proteins; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Triphosphate; Isoproterenol; Kinetics; Magnesium; Mice; Mutation; Oncogene Protein p21(ras); Serine; Tumor Cells, Cultured

1991
Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase.
    The Journal of biological chemistry, 1989, May-25, Volume: 264, Issue:15

    Topics: Adrenal Medulla; Amino Acid Sequence; Animals; Asparagine; Binding Sites; Botulinum Toxins; Cattle; GTP Phosphohydrolases; GTP-Binding Proteins; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Triphosphate; Kinetics; Membrane Proteins; Molecular Sequence Data; Peptide Fragments; Poly(ADP-ribose) Polymerases; Protein Binding; rhoB GTP-Binding Protein; Thionucleotides; Trypsin

1989
Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP.
    Molecular and cellular biology, 1988, Volume: 8, Issue:8

    Topics: Animals; Asparagine; Cell Division; Cells, Cultured; Cloning, Molecular; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Membrane Proteins; Mice; Mice, Inbred Strains; Mutation; Protein Binding; Proto-Oncogene Proteins; Proto-Oncogene Proteins p21(ras); Serine; Transfection

1988
A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein.
    The Journal of biological chemistry, 1987, Sep-25, Volume: 262, Issue:27

    Topics: Asparagine; Aspartic Acid; Cloning, Molecular; Escherichia coli; Genes; Genes, Bacterial; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Mutation; Peptide Elongation Factor Tu; Plasmids; Protein Binding

1987
Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphate.
    The Journal of biological chemistry, 1994, Sep-30, Volume: 269, Issue:39

    Topics: Adenylosuccinate Synthase; Amino Acid Sequence; Asparagine; Aspartic Acid; Base Sequence; Circular Dichroism; DNA, Complementary; Escherichia coli; GTP-Binding Proteins; Guanosine Triphosphate; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Ribonucleotides; Substrate Specificity

1994
Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms.
    Biochemistry, 1994, Apr-05, Volume: 33, Issue:13

    Topics: Asparagine; Aspartic Acid; Binding Sites; Electron Spin Resonance Spectroscopy; GTP Phosphohydrolases; GTP-Binding Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Ligands; Phosphates; Proto-Oncogene Proteins p21(ras); Recombinant Proteins; Threonine

1994
Site-directed mutagenesis of the serotonin 5-hydroxytrypamine2 receptor: identification of amino acids necessary for ligand binding and receptor activation.
    Molecular pharmacology, 1993, Volume: 43, Issue:6

    Topics: 3T3 Cells; Amphetamines; Animals; Asparagine; Aspartic Acid; Binding, Competitive; Guanosine Triphosphate; Hydrolysis; Lysergic Acid Diethylamide; Mice; Mutagenesis, Site-Directed; Phosphatidylinositols; Radioligand Assay; Receptors, Serotonin; Serotonin; Serotonin Antagonists; Serotonin Receptor Agonists

1993
Asparagine-135 of elongation factor Tu is a crucial residue for the folding of the guanine nucleotide binding pocket.
    FEBS letters, 1993, Sep-20, Volume: 330, Issue:3

    Topics: Asparagine; Base Sequence; Binding Sites; Guanosine Triphosphate; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Nucleic Acid Conformation; Oligodeoxyribonucleotides; Peptide Elongation Factor Tu; Protein Folding; Structure-Activity Relationship

1993
Analysis of the interaction of FtsZ with itself, GTP, and FtsA.
    Journal of bacteriology, 1997, Volume: 179, Issue:17

    Topics: Asparagine; Aspartic Acid; Bacillus subtilis; Bacterial Proteins; Cytoskeletal Proteins; Escherichia coli; Escherichia coli Proteins; GTP Phosphohydrolases; Guanosine Triphosphate; Mutagenesis, Site-Directed; Peptide Fragments; Polymers; Protein Binding; Recombinant Fusion Proteins; Sequence Analysis; Trypsin

1997
Contribution of Arg288 of Escherichia coli elongation factor Tu to translational functionality.
    European journal of biochemistry, 1997, Oct-15, Volume: 249, Issue:2

    Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Asparagine; Binding Sites; Conserved Sequence; Escherichia coli; GTP Phosphohydrolase-Linked Elongation Factors; Guanosine Diphosphate; Guanosine Triphosphate; Hydrogen Bonding; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Peptide Elongation Factor Tu; Protein Conformation; Recombinant Proteins; Ribosomes; RNA, Transfer, Phe; Thermus

1997
Cloning and characterization of a dominant-negative vps1 allele of the yeast Saccharomyces cerevisiae.
    Biological chemistry, 1997, Volume: 378, Issue:10

    Topics: Alanine; Alleles; Amino Acid Sequence; Animals; Asparagine; Binding Sites; Carrier Proteins; Cloning, Molecular; Gene Expression Regulation, Fungal; Genes, Fungal; GTP-Binding Proteins; Guanosine Triphosphate; Humans; Mice; Molecular Sequence Data; Rats; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Vesicular Transport Proteins

1997
Mechanism of RGS4, a GTPase-activating protein for G protein alpha subunits.
    The Journal of biological chemistry, 1998, Jan-16, Volume: 273, Issue:3

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Asparagine; Calcium-Calmodulin-Dependent Protein Kinases; GTP Phosphohydrolases; GTP-Binding Protein alpha Subunits, Gi-Go; Guanosine Triphosphate; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Protein Binding; Proteins; Rats; RGS Proteins; Saccharomyces cerevisiae; Structure-Activity Relationship

1998
The function of the p190 Rho GTPase-activating protein is controlled by its N-terminal GTP binding domain.
    The Journal of biological chemistry, 1998, Dec-18, Volume: 273, Issue:51

    Topics: 3T3 Cells; Amino Acid Sequence; Amino Acid Substitution; Animals; Asparagine; Binding Sites; Calcium-Calmodulin-Dependent Protein Kinases; Carbachol; Conserved Sequence; COS Cells; DNA-Binding Proteins; Enzyme Activation; GTPase-Activating Proteins; Guanine Nucleotide Exchange Factors; Guanosine Triphosphate; JNK Mitogen-Activated Protein Kinases; Kinetics; Mice; Mitogen-Activated Protein Kinases; Mutagenesis, Site-Directed; Nuclear Proteins; Phosphoproteins; Receptors, Muscarinic; Recombinant Proteins; Repressor Proteins; Serine; Transfection

1998
Modulation of the affinity and selectivity of RGS protein interaction with G alpha subunits by a conserved asparagine/serine residue.
    Biochemistry, 1999, Jun-15, Volume: 38, Issue:24

    Topics: Animals; Asparagine; Binding, Competitive; Conserved Sequence; Cysteine; GTP-Binding Protein alpha Subunits, Gi-Go; GTP-Binding Protein alpha Subunits, Gq-G11; GTP-Binding Proteins; GTPase-Activating Proteins; Guanosine Triphosphate; Humans; Hydrolysis; Lysine; Mutagenesis, Site-Directed; Proline; Protein Binding; Proteins; Receptors, Cell Surface; RGS Proteins; Serine

1999
Site-directed mutagenesis identifies residues in uncoupling protein (UCP1) involved in three different functions.
    Biochemistry, 2000, Mar-28, Volume: 39, Issue:12

    Topics: Adipose Tissue, Brown; Amino Acid Substitution; Animals; Asparagine; Aspartic Acid; Binding Sites; Carrier Proteins; Chlorides; Cricetinae; Electron Transport; Glutamic Acid; Glutamine; Guanosine Triphosphate; Ion Channels; Membrane Proteins; Mitochondria; Mitochondrial Proteins; Mutagenesis, Site-Directed; Protons; Saccharomyces cerevisiae; Uncoupling Agents; Uncoupling Protein 1

2000
Three-dimensional view of the surface motif associated with the P-loop structure: cis and trans cases of convergent evolution.
    Journal of molecular biology, 2000, Nov-03, Volume: 303, Issue:4

    Topics: Adenosine Triphosphate; Alanine; Amino Acid Motifs; Amino Acid Sequence; Animals; Arginine; Asparagine; Binding Sites; Conserved Sequence; Evolution, Molecular; GTP-Binding Proteins; Guanosine Triphosphate; Humans; Models, Molecular; Molecular Sequence Data; Nucleoside-Phosphate Kinase; Protein Structure, Tertiary; Ribonucleases; Sequence Alignment; Static Electricity; Substrate Specificity

2000
S111N mutation in the helical domain of human Gs(alpha) reduces its GDP/GTP exchange rate.
    Journal of cellular biochemistry, 2002, Volume: 85, Issue:3

    Topics: Adenylyl Cyclases; Aluminum Compounds; Amino Acid Substitution; Asparagine; Fluorides; GTP-Binding Protein alpha Subunits, Gs; GTP-Binding Proteins; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Diphosphate; Guanosine Triphosphate; Humans; Models, Molecular; Point Mutation; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Cell Surface; Serine; Trypsin

2002
Antiapoptotic Cdc42 mutants are potent activators of cellular transformation.
    Biochemistry, 2002, Oct-15, Volume: 41, Issue:41

    Topics: 3T3 Cells; Amino Acid Substitution; Animals; Apoptosis; Asparagine; Aspartic Acid; cdc42 GTP-Binding Protein; Cell Division; Cell Transformation, Neoplastic; COS Cells; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Mice; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Protein Binding; Trans-Activators; Transfection

2002
Signal transduction: thumbs up for inactivation.
    Nature, 2004, May-13, Volume: 429, Issue:6988

    Topics: Asparagine; Binding Sites; Catalytic Domain; GTPase-Activating Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Hydrolysis; rap1 GTP-Binding Proteins; Signal Transduction

2004
The GTPase-activating protein Rap1GAP uses a catalytic asparagine.
    Nature, 2004, May-13, Volume: 429, Issue:6988

    Topics: Adenosine Diphosphate; Aluminum Compounds; Asparagine; Binding Sites; Catalysis; Catalytic Domain; Crystallography, X-Ray; Fluorides; GTPase-Activating Proteins; Guanosine Triphosphate; Humans; Hydrolysis; Models, Molecular; Mutation; Protein Conformation; rap1 GTP-Binding Proteins; Repressor Proteins; Tuberous Sclerosis Complex 2 Protein; Tumor Suppressor Proteins

2004
Structural basis for the unique biological function of small GTPase RHEB.
    The Journal of biological chemistry, 2005, Apr-29, Volume: 280, Issue:17

    Topics: Amino Acid Sequence; Arginine; Asparagine; Binding Sites; Catalytic Domain; Cell Proliferation; Crystallography, X-Ray; Databases, Protein; GTP Phosphohydrolases; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Hydrolysis; Magnesium; Models, Molecular; Molecular Sequence Data; Monomeric GTP-Binding Proteins; Neuropeptides; Protein Conformation; Protein Kinases; Protein Structure, Secondary; Protein Structure, Tertiary; Ras Homolog Enriched in Brain Protein; ras Proteins; Repressor Proteins; Sequence Homology, Amino Acid; TOR Serine-Threonine Kinases; Tuberous Sclerosis; Tuberous Sclerosis Complex 1 Protein; Tuberous Sclerosis Complex 2 Protein; Tumor Suppressor Proteins; X-Ray Diffraction

2005
Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation.
    The Journal of biological chemistry, 2005, Jul-08, Volume: 280, Issue:27

    Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Crystallography; Enzyme Activation; Escherichia coli; Guanosine Triphosphate; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleoside-Phosphate Kinase; Phosphates; Protein Folding; Protein Structure, Quaternary; Threonine; Uridine Diphosphate; Uridine Monophosphate; Uridine Triphosphate

2005
Adenylyl cyclase Rv0386 from Mycobacterium tuberculosis H37Rv uses a novel mode for substrate selection.
    The FEBS journal, 2005, Volume: 272, Issue:12

    Topics: Adenosine Triphosphate; Adenylyl Cyclases; Amino Acid Sequence; Asparagine; Catalytic Domain; Glutamine; Guanosine Triphosphate; Isoenzymes; Molecular Sequence Data; Mutation; Mycobacterium tuberculosis; Substrate Specificity

2005
Characterization of the Rab7K157N mutant protein associated with Charcot-Marie-Tooth type 2B.
    Biochemical and biophysical research communications, 2008, Jul-25, Volume: 372, Issue:2

    Topics: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Asparagine; Cell Cycle Proteins; Charcot-Marie-Tooth Disease; Conserved Sequence; ErbB Receptors; Guanosine Triphosphate; Humans; Hydrolysis; Lysine; Mutation, Missense; Nuclear Proteins; rab GTP-Binding Proteins; rab7 GTP-Binding Proteins; RNA Interference

2008
Structure of the dominant negative S17N mutant of Ras.
    Biochemistry, 2010, Mar-09, Volume: 49, Issue:9

    Topics: Amino Acid Substitution; Asparagine; Crystallography, X-Ray; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Magnesium; Models, Molecular; Protein Binding; ras Proteins; Serine; Signal Transduction; Structure-Activity Relationship

2010
Novel pathogenic LRRK2 p.Asn1437His substitution in familial Parkinson's disease.
    Movement disorders : official journal of the Movement Disorder Society, 2010, Oct-15, Volume: 25, Issue:13

    Topics: Aged; Aged, 80 and over; Asparagine; Cell Line, Transformed; Female; Genetic Testing; Guanosine Triphosphate; Histidine; Humans; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Male; Middle Aged; Mutation; Norway; Parkinson Disease; Protein Serine-Threonine Kinases; Psychiatric Status Rating Scales; Tomography, Emission-Computed, Single-Photon; Transfection

2010